Phosphorylated α-Synuclein at Ser-129 Is Targeted to the Proteasome Pathway in a Ubiquitin-independent Manner-Reference-Cited by-同舟云学术

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Phosphorylated α-Synuclein at Ser-129 Is Targeted to the Proteasome Pathway in a Ubiquitin-independent Manner

Published:2010-12 Issue:52 Volume:285 Page:40732-40744
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Machiya Youhei,Hara Susumu,Arawaka Shigeki,Fukushima Shingo,Sato Hiroyasu,Sakamoto Masahiro,Koyama Shingo,Kato Takeo

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease

2. Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease

3. The Formation of Highly Soluble Oligomers of α-Synuclein Is Regulated by Fatty Acids and Enhanced in Parkinson's Disease

4. Tonicity-dependent induction of Sgk1 expression has a potential role in dehydration-induced natriuresis in rodents

5. Caught in the Act

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1. Physiological roles of α-synuclein serine-129 phosphorylation – not an oxymoron;Trends in Neurosciences;2024-07

2. Neuronal activity promotes secretory autophagy for the extracellular release of α-synuclein;Journal of Biological Chemistry;2024-07

3. Alpha-synuclein aggregates are phosphatase resistant;Acta Neuropathologica Communications;2024-05-31

4. USP14 regulates pS129 α-synuclein levels and oxidative stress in human SH-SY5Y dopaminergic cells;2024-05-09

5. The Role of Astrocytes and Alpha-Synuclein in Parkinson’s Disease: A Review;NeuroSci;2024-03-08

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